CAZyme Information: KDQ25952.1

Basic Information

• Species: Pleurotus ostreatus
• Lineage: Basidiomycota; Agaricomycetes; ; Pleurotaceae; Pleurotus; Pleurotus ostreatus
• CAZyme ID: KDQ25952.1
• CAZy Family: CE12
• CAZyme Description: glycoside hydrolase family 15 protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
620	KL198010|CGC3	68526.03	6.5573

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_PostreatusPC15	12460	1137138	164	12296

• Gene Location: location=KL198010:2285935-2288230(-)

Full Sequence      

MRAIQHWVIWRILPTLVAITGVSLYLSVTGNNRLLKPTNVYHELKWALYHISQHYDLPVD
AGLTEEGLVDAYIKRQTPIAQDGILANIGPNGSRCGGAKSGTVIASPSTHDPDYMYTWTR
DAALVVKLLVDQYTHNQDVSLKGIIDEYAAAQAALQKVRTPSGGMLTGGLGEPKYNIDHT
AFTEPWGRPQHDGPALRATTLLAYAKTLLKQSDRESVQQSLWPVLEKDLDYVVKYWNRTG
FDLWEEVSSSSFFTTAVQHRALREGAALARNLNKTEIAQIYSAQADNTLCFLQSYWNADI
YYVVSNTGGGRSGKDANSILASIHTFDPTAGCDATTFQPCSDKALATLYACIDAFRGLYR
INRGTAYSDAVAVGRYPEDVYMGGHPWYLTTAAVAEQLYDALYVWKSQGYIEITRISLSF
FRMVSPRIRPGTYTSARLEYHELLAEVKKFADGFIAVNAKYTPWDGSLAEQYHRDNGQPL
SARDLTWSYAASITAFNARAGALVPGGWGAKGLVVPSVCEPNPPRLVSVTFSVHAETQPG
EAIFVTGSSEALSHWSTDNAIKLSADRYPIWSGSLDVPVESALEYKYIRKADTGAVSWEQ
GSNRFLETSTKSTNVSDEWR

Enzyme Prediction     

EC	3.2.1.3:94	3.2.1.1:7	3.2.1.116:1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH15	95	495	3.5e-79	0.9529085872576177
CBM20	527	613	4.6e-27	0.9666666666666667

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
395586	Glyco_hydro_15	1.16e-121	78	497	1	417	Glycosyl hydrolases family 15. In higher organisms this family is represented by phosphorylase kinase subunits.
99883	CBM20_alpha_amylase	1.30e-31	527	620	1	95	Alpha-amylase, C-terminal CBM20 (carbohydrate-binding module, family 20) domain. This domain is found in several bacterial and fungal alpha-amylases including the maltopentaose-forming amylases (G5-amylases). Most alpha-amylases have, in addition to the C-terminal CBM20 domain, an N-terminal catalytic domain belonging to glycosyl hydrolase family 13, which hydrolyzes internal alpha-1,4-glucosidic bonds in starch and related saccharides, yielding maltotriose and maltose. Two types of soluble substrates are used by alpha-amylases including long substrates (e.g. amylose) and short substrates (e.g. maltodextrins or maltooligosaccharides). The CBM20 domain is found in a large number of starch degrading enzymes including alpha-amylase, beta-amylase, glucoamylase, and CGTase (cyclodextrin glucanotransferase). CBM20 is also present in proteins that have a regulatory role in starch metabolism in plants (e.g. alpha-amylase) or glycogen metabolism in mammals (e.g. laforin). CBM20 folds as an antiparallel beta-barrel structure with two starch binding sites. These two sites are thought to differ functionally with site 1 acting as the initial starch recognition site and site 2 involved in the specific recognition of appropriate regions of starch.
395557	CBM_20	1.89e-28	527	616	1	93	Starch binding domain.
119437	CBM20	5.34e-25	528	619	1	96	The family 20 carbohydrate-binding module (CBM20), also known as the starch-binding domain, is found in a large number of starch degrading enzymes including alpha-amylase, beta-amylase, glucoamylase, and CGTase (cyclodextrin glucanotransferase). CBM20 is also present in proteins that have a regulatory role in starch metabolism in plants (e.g. alpha-amylase) or glycogen metabolism in mammals (e.g. laforin). CBM20 folds as an antiparallel beta-barrel structure with two starch binding sites. These two sites are thought to differ functionally with site 1 acting as the initial starch recognition site and site 2 involved in the specific recognition of appropriate regions of starch.
99886	CBM20_glucoamylase	1.10e-24	523	619	3	106	Glucoamylase (glucan1,4-alpha-glucosidase), C-terminal CBM20 (carbohydrate-binding module, family 20) domain. Glucoamylases are inverting, exo-acting starch hydrolases that hydrolyze starch and related polysaccharides by releasing the nonreducing end glucose. They are mainly active on alpha-1,4-glycosidic bonds but also have some activity towards 1,6-glycosidic bonds occurring in natural oligosaccharides. The ability of glucoamylases to cleave 1-6-glycosidic binds is called "debranching activity" and is of importance in industrial applications, where complete degradation of starch to glucose is needed. Most glucoamylases are multidomain proteins containing an N-terminal catalytic domain, a C-terminal CBM20 domain, and a highly O-glycosylated linker region that connects the two. The CBM20 domain is found in a large number of starch degrading enzymes including alpha-amylase, beta-amylase, glucoamylase, and CGTase (cyclodextrin glucanotransferase). CBM20 is also present in proteins that have a regulatory role in starch metabolism in plants (e.g. alpha-amylase) or glycogen metabolism in mammals (e.g. laforin). CBM20 folds as an antiparallel beta-barrel structure with two starch binding sites. These two sites are thought to differ functionally with site 1 acting as the initial starch recognition site and site 2 involved in the specific recognition of appropriate regions of starch.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AOC97459.1|CBM20|GH15	4.82e-232	65	620	19	578
BAU78332.1|CBM20|GH15	2.31e-231	65	620	18	573
CAS91480.1|CBM20|GH15	1.65e-225	62	620	16	579
CDJ79833.1|CBM20|GH15	2.69e-225	62	620	18	583
BAL43555.1|CBM20|GH15|3.2.1.3	1.29e-221	65	620	20	576

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2VN4_A	5.46e-181	69	603	2	577	Chain A, GLUCOAMYLASE [Trichoderma reesei],2VN7_A Chain A, GLUCOAMYLASE [Trichoderma reesei]
6FRV_A	2.49e-167	69	620	3	616	Structure of the catalytic domain of Aspergillus niger Glucoamylase [Aspergillus niger]
6FHV_A	1.82e-161	67	610	6	580	Crystal structure of Penicillium oxalicum Glucoamylase [Penicillium oxalicum 114-2]
1AGM_A	8.08e-158	69	519	3	448	Refined structure for the complex of acarbose with glucoamylase from Aspergillus awamori var. x100 to 2.4 angstroms resolution [Aspergillus awamori],1DOG_A REFINED STRUCTURE FOR THE COMPLEX OF 1-DEOXYNOJIRIMYCIN WITH GLUCOAMYLASE FROM (ASPERGILLUS AWAMORI) VAR. X100 TO 2.4 ANGSTROMS RESOLUTION [Aspergillus awamori],1GLM_A REFINED CRYSTAL STRUCTURES OF GLUCOAMYLASE FROM ASPERGILLUS AWAMORI VAR. X100 [Aspergillus awamori],3GLY_A REFINED CRYSTAL STRUCTURES OF GLUCOAMYLASE FROM ASPERGILLUS AWAMORI VAR. X100 [Aspergillus awamori]
1GAH_A	8.35e-158	69	519	3	448	GLUCOAMYLASE-471 COMPLEXED WITH ACARBOSE [Aspergillus awamori]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|D8Q9M3|AMYG_SCHCM	1.22e-214	70	620	26	576	Glucoamylase ARB_02327-1 OS=Schizophyllum commune (strain H4-8 / FGSC 9210) OX=578458 GN=SCHCODRAFT_57589 PE=1 SV=1
sp|P14804|AMYG_NEUCR	1.47e-173	69	620	37	626	Glucoamylase OS=Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987) OX=367110 GN=gla-1 PE=1 SV=3
sp|P36914|AMYG_ASPOR	2.12e-172	57	620	18	612	Glucoamylase OS=Aspergillus oryzae (strain ATCC 42149 / RIB 40) OX=510516 GN=glaA PE=2 SV=2
sp|P0DN29|AMYG_ARTBC	5.80e-169	84	604	42	590	Glucoamylase ARB_02327-1 OS=Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) OX=663331 GN=ARB_02327-1 PE=1 SV=1
sp|P23176|AMYG_ASPKA	4.17e-168	63	620	21	639	Glucoamylase I OS=Aspergillus kawachii OX=1069201 GN=gaI PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000027	0.000016

TMHMM  Annotations     

Start	End
7	29